4v9l

70S Ribosome translocation intermediate FA-3.6A containing elongation factor EFG/FUSIDIC ACID/GDP, mRNA, and tRNA bound in the pe*/E state.

spinqualitylabelsall models 4v9l, resolution 3.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4v9l is a 20 chain structure with sequence from Streptomyces and Thermus thermophilus HB27. This structure supersedes the now removed PDB entries 4kd8, 4kd9, 4kda and 4kdb. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.5Å Ligands: 5OH, DPP, FUA, GDP, KBE, MG, UAL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function RS14Z_THET2 Binds 16S rRNA, required for the assembly of 30S particles and may also be responsible for determining the conformation of the 16S rRNA at the A site (By similarity). Publication Abstract from PubMed Translocation of messenger and transfer RNA (mRNA and tRNA) through the ribosome is a crucial step in protein synthesis, whose mechanism is not yet understood. The crystal structures of three Thermus ribosome-tRNA-mRNA-EF-G complexes trapped with beta,gamma-imidoguanosine 5'-triphosphate (GDPNP) or fusidic acid reveal conformational changes occurring during intermediate states of translocation, including large-scale rotation of the 30S subunit head and body. In all complexes, the tRNA acceptor ends occupy the 50S subunit E site, while their anticodon stem loops move with the head of the 30S subunit to positions between the P and E sites, forming chimeric intermediate states. Two universally conserved bases of 16S ribosomal RNA that intercalate between bases of the mRNA may act as "pawls" of a translocational ratchet. These findings provide new insights into the molecular mechanism of ribosomal translocation. Crystal structures of EF-G-ribosome complexes trapped in intermediate states of translocation.,Zhou J, Lancaster L, Donohue JP, Noller HF Science. 2013 Jun 28;340(6140):1236086. doi: 10.1126/science.1236086. PMID:23812722 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Elongation factor 3D structures Ribosome 3D structures

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